Identification of amyloid-β binding sites using an antisense peptide approach

Abstract
The amyloid-beta (A beta) peptide is a cytotoxic peptide implicated in the pathology of Alzheimer's disease (AD). Catalase and the endoplasmic reticulum A beta binding dehydrogenase (ERAB) are both inhibited by characterized fragments of the A beta peptide. In order to target such proteins it is essential to determine which components of these enzymes interact with A beta. This study reports the use of antisense peptide methodology to identify specific A beta-binding domains. Synthetic peptides corresponding to the regions of catalase and ERAB identified showed specific binding to A beta and also prevented A beta cytotoxicity. Antisense peptide methodology has identified A beta recognition sequences and may also be applied to the identification of novel A beta protein interactions to identify targets for use in the treatment of AD.
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